Dystroglycan in the Cerebellum is a Laminin α2‐chain Binding Protein at the Glial‐Vascular Interface and is Expressed in Purkinje cells

  title={Dystroglycan in the Cerebellum is a Laminin $\alpha$2‐chain Binding Protein at the Glial‐Vascular Interface and is Expressed in Purkinje cells},
  author={Min Tian and Christian Jacobson and Stephen H. Gee and Kevin P. Campbell and Salvatore Carbonetto and Mathias Jucker},
  journal={European Journal of Neuroscience},
Dystroglycan is a core component of the dystrophin receptor complex in skeletal muscle which links the extracellular matrix to the muscle cytoskeleton. Dystrophin, dystrophin‐related protein (DRP, utrophin) and dystroglycan are present not only in muscles but also in the brain. Dystrophin is expressed in certain neuronal populations while DRP is associated with perivascular astrocytes. To gain insights into the function and molecular interactions of dystroglycan in the brain, we examined the… 

Dystroglycan contributes to the formation of multiple dystrophin‐like complexes in brain

In the brain, unlike in muscle, the association of syntrophin with dystrophin is not crucial for the DAP complex which suggests that it may be associated with other proteins.

A stoichiometric complex of neurexins and dystroglycan in brain

The data indicate that dystroglycan is a physiological ligand for neURExins and that neurexins' tightly regulated interaction could mediate cell adhesion between brain cells.

Brain dystrophin-glycoprotein complex: Persistent expression of beta-dystroglycan, impaired oligomerization of Dp71 and up-regulation of utrophins in animal models of muscular dystrophy

This suggests an association of β-dystroglycan with membranes at the vascular-glial interface in the forebrain, and abnormal oligomerization of the dystrophin isoform Dp71 might be involved in the pathophysiological mechanisms underlying abnormal brain functions.

Subcellular concentration of β‐dystroglycan in photoreceptors and glial cells of the chick retina

Results show that in the retina β‐dystroglycan is exclusively expressed by photoreceptors and glial cells and that α1B subunit of the N‐type voltage‐gated calcium channel in the outer plexiform layer indicates that both proteins might be part of a macromolecular complex.

Assembly of a perivascular astrocyte protein scaffold at the mammalian blood–brain barrier is dependent on α‐syntrophin

It is concluded that α‐syntrophin is a central organizer of the astrocyte dystrophin complex, an important molecular scaffold for localization of aquaporin‐4 at the blood–brain barrier.

Identification of dystroglycan as a second laminin receptor in oligodendrocytes, with a role in myelination

It is reported that the myelinating glia of the CNS, oligodendrocytes, express and use dystroglycan receptors to regulate myelin formation, and this results indicate that laminins are likely to regulate central nervous system myelination by interacting with both integrin receptors and dyStrogly can receptors.

Dystroglycan Is Selectively Associated with Inhibitory GABAergic Synapses But Is Dispensable for Their Differentiation

Dystroglycan is the first identified adhesive macromolecule at mature GABA synapses and is likely to function in modulating inhibitory synapses or conferring specialized properties on a subset of them.

Distribution of Dystroglycan in Normal Adult Mouse Tissues

It is suggested that dystroglycan is involved in linking basement membranes to epithelial and muscle cells and may be important for the maintenance of tissue integrity.



β‐Dystroglycan: Subcellular Localisation in Rat Brain and Detection of a Novel Immunologically Related, Postsynaptic Density‐Enriched Protein

Preabsorption of the antiserum with the antigen abolished reactivity against both β‐dystroglycan and the 164‐kDa postsynaptic density‐enriched protein, confirming that the two species are immunologically related.

Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle

The results could provide a basis for the upregulation of DRP as a potential therapeutic approach in Duchenne muscular dystrophy and mdx muscle.

Dystroglycan: brain localisation and chromosome mapping in the mouse.

In situ hybridisation to mouse brain sections shows that the dystroglycan gene is expressed in relatively few structures and co-localises with dystrophin mRNA in hippocampus, dentate gyrus, olfactory bulb and Purkinje neurons but, surprisingly, not in the cortex.

Non-muscle alpha-dystroglycan is involved in epithelial development

It is shown that dystroglycan during mouse development in nonmuscle tissues is expressed in epithelium, and it is suggested that the dystoglycan complex acts as a receptor for basement membrane components during epithelial morphogenesis.

The subcellular distribution of chromosome 6-encoded dystrophin-related protein in the brain

The distribution of DRP is conserved across a large evolutionary distance, from mammals to elasmobranchs, suggesting that DRP may play a role in the maintenance of regional specializations in the brain.

Interaction of chromosome-6-encoded dystrophin related protein with the extracellular matrix.

The data suggest that dystrophin-related protein may function in the generation and maintenance of regional substratum-associated membrane specializations, such as those found at the blood-brain barrier.

A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin

The results support a role for the striated muscle dystrophin-glycoprotein complex in linking the actin- based cytoskeleton with the extracellular matrix and suggest that dystophin and dystroglycan may play substantially different functional roles in nonmuscle tissues.

Purification of Cranin, a Laminin Binding Membrane Protein

It is found that brain α-dystroglycan is tightly associated with membranes, and localizes to regions of synaptic contact as assessed by immunocytochemistry of rat cerebellum, and it is shown that chondroitin sulfate and heparan sulfate are not critical for laminin binding, and indeed are apparently not expressed at all in dystrogelcan from CHO cells.

Detection of dystrophin in the postsynaptic density of rat brain and deficiency in a mouse model of Duchenne muscular dystrophy.

The results indicate that brain dystrophins are localized to the PSD, potentially as three isoforms, and raise the possibility that cognitive abnormalities in DMD are attributable to synaptic dysfunction associated with deficits in brain Dystrophin molecules.